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Microbial glucoamylases: structural and functional properties and biotechnological uses

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Abstract

Glucoamylases (GAs) are one of the principal groups of enzymes involved in starch hydrolysis and belong to the glycosylhydrolase family. They are classified as exo-amylases due to their ability to hydrolyze α-1,4 glycosidic bonds from the non-reducing end of starch, maltooligosaccharides, and related substrates, releasing β-D-glucose. Structurally, GAs possess a characteristic catalytic domain (CD) with an (α/α)6 fold and exhibit five conserved regions within this domain. The CD may or may not be linked to a non-catalytic domain with variable functions depending on its origin. GAs are versatile enzymes with diverse applications in food, biofuel, bioplastic and other chemical industries. Although fungal GAs are commonly employed for these purposes, they have limitations such as their low thermostability and an acidic pH requirement. Alternatively, GAs derived from prokaryotic organisms are a good option to save costs as they exhibit greater thermostability compared to fungal GAs. Moreover, a group of cold-adapted GAs from psychrophilic organisms demonstrates intriguing properties that make them suitable for application in various industries. This review provides a comprehensive overview of the structural and sequential properties as well as biotechnological applications of GAs in different industrial processes.

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Acknowledgements

NMW is a doctoral fellow from CONICET. MM, MVB and DFGC are research scientists from CONICET.

Funding

This work was supported by ANPCyT (PICT 2018 01440), National University of Rosario (VT-2021) and CONICET (PIP 2021–3068).

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Authors and Affiliations

  1. CEFOBI–CONICET. Centro de Estudios Fotosintéticos y Bioquímicos - Consejo Nacional de Investigaciones Científicas y Técnicas. Facultad de Ciencias Bioquímicas y Farmacéuticas, Universidad Nacional de Rosario, Suipacha 531, Rosario, Santa Fe, Argentina

    Natael M. Wayllace, Mariana Martín, María V. Busi & Diego F. Gomez-Casati

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  1. Natael M. Wayllace
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  2. Mariana Martín
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  3. María V. Busi
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  4. Diego F. Gomez-Casati
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Contributions

Writing original draft: NMW; writing, review and editing: DFGC, MVB and MM. We searched databases (Pubmed and Scopus) for keywords such as glucoamylase, glucoside hydrolase, microbial glucoamylases, glucoamylase structure and biotechnological applications of glucoamylases.

Corresponding authors

Correspondence to María V. Busi or Diego F. Gomez-Casati.

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Wayllace, N.M., Martín, M., Busi, M.V. et al. Microbial glucoamylases: structural and functional properties and biotechnological uses. World J Microbiol Biotechnol 39, 293 (2023). https://doi.org/10.1007/s11274-023-03731-z

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